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1ujw

From Proteopedia

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Current revision

Structure of the complex between BtuB and Colicin E3 Receptor binding domain

Structural highlights

1ujw is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.75Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BTUB_ECOLI Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins.[HAMAP-Rule:MF_01531]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Cellular import of colicin E3 is initiated by the Escherichia coli outer membrane cobalamin transporter, BtuB. The 135-residue 100-A coiled-coil receptor-binding domain (R135) of colicin E3 forms a 1:1 complex with BtuB whose structure at a resolution of 2.75 A is reported. Binding of R135 to the BtuB extracellular surface (DeltaG(o) = -12 kcal mol(-1)) is mediated by 27 residues of R135 near the coiled-coil apex. Formation of the R135-BtuB complex results in unfolding of R135 N- and C-terminal ends, inferred to be important for unfolding of the colicin T-domain. Small conformational changes occur in the BtuB cork and barrel domains but are insufficient to form a translocation channel. The absence of a channel and the peripheral binding of R135 imply that BtuB serves to bind the colicin, and that the coiled-coil delivers the colicin to a neighboring outer membrane protein for translocation, thus forming a colicin translocon. The translocator was concluded to be OmpF from the occlusion of OmpF channels by colicin E3.

The structure of BtuB with bound colicin E3 R-domain implies a translocon.,Kurisu G, Zakharov SD, Zhalnina MV, Bano S, Eroukova VY, Rokitskaya TI, Antonenko YN, Wiener MC, Cramer WA Nat Struct Biol. 2003 Nov;10(11):948-54. Epub 2003 Oct 5. PMID:14528295^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kurisu G, Zakharov SD, Zhalnina MV, Bano S, Eroukova VY, Rokitskaya TI, Antonenko YN, Wiener MC, Cramer WA. The structure of BtuB with bound colicin E3 R-domain implies a translocon. Nat Struct Biol. 2003 Nov;10(11):948-54. Epub 2003 Oct 5. PMID:14528295 doi:10.1038/nsb997

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ujw"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ujw' size='340' side='right'caption='[[1ujw]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ujw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UJW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UJW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ujw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UJW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UJW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AAE:ACETOACETIC+ACID'>AAE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GP1:GLUCOSAMINE+1-PHOSPHATE'>GP1</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=LIM:3-OXO-PENTADECANOIC+ACID'>LIM</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1nqe|1nqe]], [[1jch|1jch]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AAE:ACETOACETIC+ACID'>AAE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GP1:GLUCOSAMINE+1-PHOSPHATE'>GP1</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=LIM:3-OXO-PENTADECANOIC+ACID'>LIM</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ujw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ujw OCA], [https://pdbe.org/1ujw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ujw RCSB], [https://www.ebi.ac.uk/pdbsum/1ujw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ujw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/BTUB_ECOLI BTUB_ECOLI]] Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins.[HAMAP-Rule:MF_01531] [[https://www.uniprot.org/uniprot/CEA3_ECOLX CEA3_ECOLX]] Inactivates ribosomes by hydrolyzing 16S RNA in 30S ribosomes at a specific site.  Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
+[https://www.uniprot.org/uniprot/BTUB_ECOLI BTUB_ECOLI] Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins.[HAMAP-Rule:MF_01531]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Antonenko, Y N]]
+[[Category: Antonenko YN]]
-[[Category: Bano, S]]
+[[Category: Bano S]]
-[[Category: Cramer, W A]]
+[[Category: Cramer WA]]
-[[Category: Eroukova, V Y]]
+[[Category: Eroukova VY]]
-[[Category: Kurisu, G]]
+[[Category: Kurisu G]]
-[[Category: Rokitskaya, T I]]
+[[Category: Rokitskaya TI]]
-[[Category: Wiener, M C]]
+[[Category: Wiener MC]]
-[[Category: Zakharov, S D]]
+[[Category: Zakharov SD]]
-[[Category: Zhalnina, M V]]
+[[Category: Zhalnina MV]]
-[[Category: Beta-barrel]]
-[[Category: Coiled-coil]]
-[[Category: Transport protein-hydrolase complex]]

1ujw

From Proteopedia

Current revision

Structure of the complex between BtuB and Colicin E3 Receptor binding domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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